GDIs: central regulatory molecules in Rho GTPase activation

Trends Cell Biol. 2005 Jul;15(7):356-63. doi: 10.1016/j.tcb.2005.05.001.

Abstract

The GDP dissociation inhibitors (GDIs) are pivotal regulators of Rho GTPase function. GDIs control the access of Rho GTPases to regulatory guanine nucleotide exchange factors and GTPase-activating proteins, to effector targets and to membranes where such effectors reside. We discuss here our current understanding of how Rho GTPase-GDI complexes are regulated by various proteins, lipids and enzymes that exert GDI displacement activity. We propose that phosphorylation mediated by diverse kinases might provide a means of controlling and coordinating Rho GTPase activation.

Publication types

  • Review

MeSH terms

  • Animals
  • Enzyme Activators / pharmacology
  • Guanine Nucleotide Dissociation Inhibitors / metabolism*
  • Guanine Nucleotide Dissociation Inhibitors / physiology*
  • Guanine Nucleotide Exchange Factors / pharmacology
  • Humans
  • Lipids / pharmacology
  • Phosphorylation
  • Protein Kinases / metabolism*
  • Proteins / physiology
  • Tumor Suppressor Proteins
  • rab GTP-Binding Proteins / metabolism*
  • rho GTP-Binding Proteins / antagonists & inhibitors
  • rho GTP-Binding Proteins / chemistry
  • rho GTP-Binding Proteins / metabolism*
  • rho GTP-Binding Proteins / physiology
  • rho Guanine Nucleotide Dissociation Inhibitor gamma
  • rho-Specific Guanine Nucleotide Dissociation Inhibitors

Substances

  • ARHGDIG protein, human
  • Enzyme Activators
  • GDP dissociation inhibitor 1
  • Guanine Nucleotide Dissociation Inhibitors
  • Guanine Nucleotide Exchange Factors
  • Lipids
  • Proteins
  • Tumor Suppressor Proteins
  • rho Guanine Nucleotide Dissociation Inhibitor gamma
  • rho-Specific Guanine Nucleotide Dissociation Inhibitors
  • Protein Kinases
  • rab GTP-Binding Proteins
  • rho GTP-Binding Proteins